The scaffolding protein CASK mediates the interaction between rabphilin3a and β‐neurexins

Zhang, Yan; Luan, Zhidong; Liu, Aihua; Hu, Gengxi

doi:10.1016/s0014-5793(01)02450-4

Cited by 41 publications

(38 citation statements)

References 26 publications

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“…Second, NRXN1 knockdown in INS-E cells and KO in mouse islets impairs secretory granule docking. Third, given the extensive resemblance between regulated secretion in neurons and in the ␤ cell, the known importance of interactions involving NRXN in synaptic vesicle docking at the presynaptic membrane suggests a similar role for NRXN in ␤ cells (16,24,25). In neurons, the interaction between NRXN and the granuphilin-related protein rabphilin-3 is mediated by the intermediary protein CASK (24), a known NRXN binding partner (17,18,45).…”

Section: Discussionmentioning

confidence: 99%

“…In neurons, NRXNs likely contribute to synaptic vesicle docking via interactions with rabphilin-3A (24). ␤ cells express the rabphilin-3-like protein granuphilin, which associates with secretory granules (27).…”

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

“…In vitro work suggests that NRXNs interact with the synaptic vesicle-associated protein rabphilin-3A via CASK (24) and contribute to synaptic vesicle docking (16,25). ␤ cells also express CASK (19) and, in addition, granuphilin, a rabphilin-3 homologue implicated in insulin granule docking (26,27).…”

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confidence: 99%

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Neurexin-1α Contributes to Insulin-containing Secretory Granule Docking

Mosedale

Egodage

Calma

et al. 2012

Journal of Biological Chemistry

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Background:The cell surface, transmembrane protein neurexin may play a role in insulin secretion. Results: Knockdown and knock-out of neurexin-1␣, the predominant ␤-cell isoform, increased insulin secretion and impaired secretory granule docking. Conclusion: Neurexin-1␣ helps mediate insulin granule docking and thereby constrains secretion. Significance: Neurexin-1␣ could couple localization and functioning of the insulin docking and secretory machinery to extracellular protein interactions.

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Section: Discussionmentioning

confidence: 99%

Section: Journal Of Biological Chemistrymentioning

confidence: 99%

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Neurexin-1α Contributes to Insulin-containing Secretory Granule Docking

Mosedale

Egodage

Calma

et al. 2012

Journal of Biological Chemistry

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“…Kif13B kinesin is a plus end motor protein that in neurons transports PIP 3 -containing vesicle along microtubules, thus promoting neuronal polarity (Horiguchi et al, 2006). The exocyst is a complex of eight proteins in mammals involved in the posttranslational regulation of protein synthesis and polarized membrane domain formation, which is often mediated by multidomain scaffold interactions (Zhang et al, 2001;Inoue et al, 2003Inoue et al, , 2006Hsu et al, 2004;Anitei et al, 2006;Gerges et al, 2006;Elias and Nicoll, 2007;Gorczyca et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

Dlg1, Sec8, and Mtmr2 Regulate Membrane Homeostasis in Schwann Cell Myelination

Bolis¹,

Coviello²,

Visigalli³

et al. 2009

Journal of Neuroscience

109

102

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How membrane biosynthesis and homeostasis is achieved in myelinating glia is mostly unknown. We previously reported that loss of myotubularin-related protein 2 (MTMR2) provokes autosomal recessive demyelinating Charcot-Marie-Tooth type 4B1 neuropathy, characterized by excessive redundant myelin, also known as myelin outfoldings. We generated a Mtmr2-null mouse that models the human neuropathy. We also found that, in Schwann cells, Mtmr2 interacts with Discs large 1 (Dlg1), a scaffold involved in polarized trafficking and membrane addition, whose localization in Mtmr2-null nerves is altered. We here report that, in Schwann cells, Dlg1 also interacts with kinesin 13B (kif13B) and Sec8, which are involved in vesicle transport and membrane tethering in polarized cells, respectively. Taking advantage of the Mtmr2-null mouse as a model of impaired membrane formation, we provide here the first evidence for a machinery that titrates membrane formation during myelination. We established Schwann cell/DRG neuron cocultures from Mtmr2-null mice, in which myelin outfoldings were reproduced and almost completely rescued by Mtmr2 replacement. By exploiting this in vitro model, we propose a mechanism whereby kif13B kinesin transports Dlg1 to sites of membrane remodeling where it coordinates a homeostatic control of myelination. The interaction of Dlg1 with the Sec8 exocyst component promotes membrane addition, whereas with Mtmr2, negatively regulates membrane formation. Myelin outfoldings thus arise as a consequence of the loss of negative control on the amount of membrane, which is produced during myelination.

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“…It is currently unknown how mLin-7C localizes at the nectin-based cell ± cell junctions, but the present results indicate that mLin-7C is associated with afadin or ZO-1 indirectly through an unknown molecule in an actin cytoskeleton-independent manner. mLin-7C forms a ternary complex with mLin-2 and mLin-10 (Borg et al, 1998;Butz et al, 1998) and each of these molecules interacts with many other molecules: mLin-7 with PSD-95, type 2 NMDA receptors, BGT-1, Pals, b-catenin, and VAM-1 (Jo et al, 1999;Perego et al, 1999Perego et al, , 2000Kamberov et al, 2000;Tseng et al, 2001); mLin-2 with neurexin, syndecan, protein 4.1, calcium channels, Tbr-1, hDlg, JAM, and rabphilin3A (Hata et al, 1996;Cohen et al, 1998;Hsueh et al, 1998Hsueh et al, , 2000Maximov et al, 1999;Nix et al, 2000;Martinez-Estrada et al, 2001;Zhang et al, 2001); and mLin-10 with amyloid precursor protein, Munc-18, neurexins, and KIF17 (Borg et al, 1996;Okamoto and SuÈ dhof, 1997;Biederer and SuÈ dhof, 2000;Setou et al, 2000). These earlier observations together with the present results suggest that these proteins directly or indirectly binding to mLin-7 are recruited to the nectinbased cell ± cell junctions.…”

Section: Discussionmentioning

confidence: 99%

Localization of mLin-7 at nectin-based cell–cell junctions

et al. 2002

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In C. elegans, lin-7 as well as lin-2/lin-10 is involved in the proper localization of the LET-23 receptor tyrosine kinase that regulates vulval induction. The mammalian homologue, mLin-7, forms a ternary complex with the mammalian homologues of LIN-2 and LIN-10 and localizes at cell ± cell junctions in epithelial cells, but the mechanism of this localization of mLin-7 is unknown. Nectin is an immunoglobulin-like cell ± cell adhesion molecule that is involved in organization of adherens and tight junctions in epithelial cells. Nectin is indirectly associated with the cadherin ± catenin system and the actin cytoskeleton through afadin, an actin ®lament-binding protein. We showed here that mLin-7 localized at the nectin-based cell ± cell junctions. This localization of mLin-7 required the interaction of nectin with afadin, but not the cadherin ± catenin system or the actin cytoskeleton. mLin-7 did not directly interact with nectin or afadin. The results indicate that mLin-7 localizes at cell ± cell junctions through the nectin ± afadin system.

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The scaffolding protein CASK mediates the interaction between rabphilin3a and β‐neurexins

Cited by 41 publications

References 26 publications

Neurexin-1α Contributes to Insulin-containing Secretory Granule Docking

Neurexin-1α Contributes to Insulin-containing Secretory Granule Docking

Dlg1, Sec8, and Mtmr2 Regulate Membrane Homeostasis in Schwann Cell Myelination

Localization of mLin-7 at nectin-based cell–cell junctions

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